title: Biosynthesis of complex iron-sulfur enzymes.
abstract: Recent advances in our understanding of the mechanisms for the biosynthesis of the complex iron-sulfur (Fe-S) containing prosthetic groups associated with [FeFe]-hydrogenases and nitrogenases have revealed interesting parallels. The biosynthesis of the H-cluster ([FeFe]-hydrogenase) and the FeMo-co (nitrogenase) occurs through a coordinated process that involves the modification of Fe-S cluster precursors synthesized by the general host cell machinery (Isc/Suf). Key modifications to the Fe-S precursors are introduced by the activity of radical S-adenosylmethionine (SAM) enzymes on unique scaffold proteins. The transfer of the modified clusters to a cofactor-less structural apo-protein completes maturation. Together these features provide the basis for establishing unifying paradigms for complex Fe-S cluster biosynthesis for these enzymes.
authors.affiliation: The Astrobiology Biogeocatalysis Research Center and the Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, United States.
authors.forename: Eric M
authors.initials: EM
authors.lastname: Shepard
authors.forename: Eric S
authors.initials: ES
authors.lastname: Boyd
authors.forename: Joan B
authors.initials: JB
authors.lastname: Broderick
authors.forename: John W
authors.initials: JW
authors.lastname: Peters
mesh_terms: D000818:Animals; D001419:Bacteria / Q000201:enzymology; D001426:Bacterial Proteins / Q000378:metabolism; D006801:Humans; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D014176:Protein Biosynthesis
chemical_list: D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins